Mov34, p39B, l(2)k08003
1.4 (northern blot)
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Rpn8 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Rpn8 in GBrowse 2
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Source for merge of: Mov34 l(2)k08003
The nomenclature of genes encoding subunits of the 26S proteasome of D. melanogaster have been standardized according to FBrf0215459. These symbols/names largely follow those used already in FlyBase, and largely mirror fly community usage. HOWEVER, note that at least one other nomenclature system exists that is followed by the HUGO Gene Nomenclature Committee (HGNC), for example, with the unfortunate result that several D. melanogaster genes have shared synonyms.
RNAi screen using dsRNA made from templates generated with primers directed against this gene results in the formation of short, monastral bipolar spindles and severe proliferation defects when assayed in S2 cells. This phenotype can be observed when the screen is performed with or without Cdc27 dsRNA.
RNAi generated by PCR using primers directed to this gene causes a cell growth and viability phenotype when assayed in Kc167 and S2R+ cells.
RNAi screen using dsRNA made from templates generated with primers directed against this gene causes a cell growth and viability phenotype when assayed in Kc167 and S2R+ cells.
The 26S proteolytic complex, a multiprotein complex containing many subunits (including those encoded by Pros26.4, Pros54 and Mov34), can be assembled from two smaller multiprotein complexes, the μ particle and the 20S proteasome, by a process that requires ATP.